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Reviewed, UniProtKB/Swiss-Prot Q2YMD1 (PDXH_BRUA2)

Last modified November 25, 2008. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pyridoxine/pyridoxamine 5'-phosphate oxidase
    EC=1.4.3.5
Alternative name(s):
    PNP/PMP oxidase
      Short name=PNPOx
    Pyridoxal 5'-phosphate synthase
Gene names
Name: pdxH
Ordered Locus Names: BAB1_0444
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) By similarity.

Catalytic activity

Pyridoxamine 5'-phosphate + H(2)O + O(2) = pyridoxal 5'-phosphate + NH(3) + H(2)O(2).

Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'-phosphate + H(2)O(2).

Cofactor

Binds 1 FMN per subunit By similarity.

Pathway

Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.

Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the pyridoxamine 5'-phosphate oxidase family.

Ontologies

Keywords

   Biological processPyridoxine biosynthesis
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

pyridoxine biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionFMN binding

Inferred from electronic annotation. Source: HAMAP

pyridoxamine-phosphate oxidase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 208208Pyridoxine/pyridoxamine 5'-phosphate oxidase
PRO_0000255856

Regions

Nucleotide binding70 – 712FMN By similarity
Nucleotide binding134 – 1352FMN By similarity
Region185 – 1873Substrate binding By similarity

Sites

Binding site551FMN By similarity
Binding site581FMN; via amide nitrogen By similarity
Binding site601Substrate By similarity
Binding site771FMN By similarity
Binding site1171Substrate By similarity
Binding site1211Substrate By similarity
Binding site1251Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YMD1-1 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: CB1F50BC9612DE28

FASTA20823,866
        10         20         30         40         50         60 
MEPVKMTNSS DDFTQSAEPF KLFAEWLADA AKSEPNDPNA VALATVDPDG LPNVRMVLLK 

        70         80         90        100        110        120 
DFDETGFVFY TNYESKKGQE ILSAEKAAMC FHWKSLRRQV RVRGPVEKVS DAEADAYYAS 

       130        140        150        160        170        180 
RPRGSRIGAW ASKQSRPLES RFALEKAVAE YTAKYAIGDI PRPPYWSGFR IRPVSIEFWH 

       190        200 
DRPFRLHDRV LFTRPTPEGD WNKDRLYP 

« Hide

References

[1]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed: 16299333] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM040264 Genomic DNA. Translation: CAJ10400.1.
RefSeqYP_413904.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3788842.
GenomeReviewsGene locus BAB1_0444 in contig AM040264_GR.
KEGGbmf:BAB1_0444.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2YMD1.

Enzyme and pathway databases

BioCycBMEL359391:BAB1_0444-MON.

Family and domain databases

HAMAPMF_01629.
[Tree]
InterProIPR011576. PNPOx_rel_FMN_bd_core.
IPR000659. Pyridox_oxidase.
IPR012349. Split_barrel_FMN_bd.
[Graphical view]
Gene3DG3DSA:2.30.110.10. PNPOx_FMN_bd. 1 hit.
PANTHERPTHR10851. Pyridox_oxidase. 1 hit.
PfamPF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
ProDomPD006312. Pyridox_oxidase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00558. pdxH. 1 hit.
PROSITEPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXH_BRUA2
AccessionPrimary (citable) accession number: Q2YMD1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: February 7, 2006
Last modified: November 25, 2008
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents